In vivo developmental studies of Helicoverpa armigera and in silico molecular interactions with trypsin reveal the bio-insecticidal potential of trypsin inhibitor (SSTI) isolated from Solanum surattense.

Autor: Herwade AP; Department of Biotechnology, Shivaji University, Kolhapur 416004, MS, India., Barale SS; Department of Microbiology, Shivaji University, Kolhapur 416004, MS, India., Sonawane KD; Department of Microbiology, Shivaji University, Kolhapur 416004, MS, India; Structural Bioinformatics Unit, Department of Biochemistry, Shivaji University, Kolhapur 416004, MS, India; Department of Biochemistry, Shivaji University, Kolhapur 416004, MS, India; Department of Chemistry, Shivaji University, Kolhapur 416004, MS, India., Pawar PK; Department of Biochemistry, Shivaji University, Kolhapur 416004, MS, India. Electronic address: pkp.biochem@unishivaji.ac.in.
Jazyk: angličtina
Zdroj: International journal of biological macromolecules [Int J Biol Macromol] 2022 Dec 31; Vol. 223 (Pt A), pp. 335-345. Date of Electronic Publication: 2022 Oct 28.
DOI: 10.1016/j.ijbiomac.2022.10.226
Abstrakt: We report the impact of gut protease inhibition on the development of Helicoverpa armigera by trypsin inhibitor and the use of molecular modeling to understand the mechanism of trypsin inhibition. Larvae of H. armigera fed on an artificial diet containing 150 and 300 μg/ml SSTI showed a negative impact on the insects' development in terms of mean larval weight, larval fatality, survival rate, and nutritional indices. Prominent physical abnormalities like curled wings, malformed appendages, and small body size were observed during the development. Gene expression studies revealed down regulation in trypsin (HaTry 1, 2, 3, 4, 6, 8) and chymotrypsin (HaChy 1, 2, 3, 4) genes of the larval gut upon treatment of SSTI. Homology modeling has been used to build the three-dimensional structure of SSTI, which showed β-sheets having a stable canonical inhibitory loop (CIL) with conserved lysine residue. Molecular docking studies showed the strong binding of SSTI at the active site of trypsin. Molecular dynamic (MD) simulation revealed the stable interactions of the rigid CIL of SSTI at the active site of trypsin, leading to its destabilization. Conserved lysine63 of the P1 site in SSTI forms a strong hydrogen bonding network with residues Asp189 and Ser190 of trypsin.
Competing Interests: Declaration of competing interest The authors declare that they have no conflicts of interest.
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Databáze: MEDLINE
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